Browse by DISSEMINATION: Published

SASDX95 – DNA repair protein RAD51 homolog 1 (RAD51) [F86E, A89E] in complex with Breast cancer type 2 susceptibility protein (BRCA2) truncation containing the second, third and fourth BRC repeats (BRC2-4) at 1 mg/mL

Breast cancer type 2 susceptibility protein (BRC repeats 2-4)DNA repair protein RAD51 homolog 1 (F86E A89E) experimental SAS data
Breast cancer type 2 susceptibility protein (BRC repeats 2-4) DNA repair protein RAD51 homolog 1 (F86E A89E) Kratky plot
Sample: Breast cancer type 2 susceptibility protein (BRC repeats 2-4) monomer, 39 kDa Homo sapiens protein
DNA repair protein RAD51 homolog 1 (F86E A89E) trimer, 111 kDa Homo sapiens protein
Buffer: 20 mM K₂HPO₄/KH₂PO₄, 100 mM NaCl, 200 mM Li₂SO₄, 5% glycerol, 1 mM DTT, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 Dec 2
Breaking new ground into RAD51–BRC repeats interplay in Homologous Recombination (2025)
Rinaldi F, Franco P, Veronesi M, Romeo E, Bresciani V, Varignani G, Catalano F, Bernetti M, Masetti M, Langer J, Girotto S, Cavalli A
RgGuinier 6.5 nm
Dmax 28.5 nm
VolumePorod 334 nm3

SASDXA5 – DNA repair protein RAD51 homolog 1 (RAD51) [F86E, A89E] in complex with Breast cancer type 2 susceptibility protein (BRCA2) truncation containing the second, third and fourth BRC repeats (BRC2-4) at 2 mg/mL

Breast cancer type 2 susceptibility protein (BRC repeats 2-4)DNA repair protein RAD51 homolog 1 (F86E A89E) experimental SAS data
Breast cancer type 2 susceptibility protein (BRC repeats 2-4) DNA repair protein RAD51 homolog 1 (F86E A89E) Kratky plot
Sample: Breast cancer type 2 susceptibility protein (BRC repeats 2-4) monomer, 39 kDa Homo sapiens protein
DNA repair protein RAD51 homolog 1 (F86E A89E) trimer, 111 kDa Homo sapiens protein
Buffer: 20 mM K₂HPO₄/KH₂PO₄, 100 mM NaCl, 200 mM Li₂SO₄, 5% glycerol, 1 mM DTT, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 Dec 2
Breaking new ground into RAD51–BRC repeats interplay in Homologous Recombination (2025)
Rinaldi F, Franco P, Veronesi M, Romeo E, Bresciani V, Varignani G, Catalano F, Bernetti M, Masetti M, Langer J, Girotto S, Cavalli A
RgGuinier 6.5 nm
Dmax 28.5 nm
VolumePorod 473 nm3

SASDXB5 – DNA repair protein RAD51 homolog 1 (RAD51) [F86E, A89E] in complex with Breast cancer type 2 susceptibility protein (BRCA2) truncation containing the second, third and fourth BRC repeats (BRC2-4) at 3.5 mg/mL

Breast cancer type 2 susceptibility protein (BRC repeats 2-4)DNA repair protein RAD51 homolog 1 (F86E A89E) experimental SAS data
Breast cancer type 2 susceptibility protein (BRC repeats 2-4) DNA repair protein RAD51 homolog 1 (F86E A89E) Kratky plot
Sample: Breast cancer type 2 susceptibility protein (BRC repeats 2-4) monomer, 39 kDa Homo sapiens protein
DNA repair protein RAD51 homolog 1 (F86E A89E) trimer, 111 kDa Homo sapiens protein
Buffer: 20 mM Hepes, 350 mM KCl, 1 mM DTT, 5% Glycerol, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 Dec 4
Breaking new ground into RAD51–BRC repeats interplay in Homologous Recombination (2025)
Rinaldi F, Franco P, Veronesi M, Romeo E, Bresciani V, Varignani G, Catalano F, Bernetti M, Masetti M, Langer J, Girotto S, Cavalli A
RgGuinier 6.9 nm
Dmax 28.5 nm
VolumePorod 652 nm3

SASDXC5 – DNA repair protein RAD51 homolog 1 (RAD51) [F86E, A89E] in complex with Breast cancer type 2 susceptibility protein (BRCA2) truncation containing the second, third and fourth BRC repeats (BRC2-4) at 7 mg/mL

Breast cancer type 2 susceptibility protein (BRC repeats 2-4)DNA repair protein RAD51 homolog 1 (F86E A89E) experimental SAS data
Breast cancer type 2 susceptibility protein (BRC repeats 2-4) DNA repair protein RAD51 homolog 1 (F86E A89E) Kratky plot
Sample: Breast cancer type 2 susceptibility protein (BRC repeats 2-4) monomer, 39 kDa Homo sapiens protein
DNA repair protein RAD51 homolog 1 (F86E A89E) trimer, 111 kDa Homo sapiens protein
Buffer: 20 mM Hepes, 350 mM KCl, 1 mM DTT, 5% Glycerol, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 Dec 4
Breaking new ground into RAD51–BRC repeats interplay in Homologous Recombination (2025)
Rinaldi F, Franco P, Veronesi M, Romeo E, Bresciani V, Varignani G, Catalano F, Bernetti M, Masetti M, Langer J, Girotto S, Cavalli A
RgGuinier 6.8 nm
Dmax 28.3 nm
VolumePorod 542 nm3

SASDXH2 – Mammalian translation elongation factor eEF1A2

Mammalian translation elongation factor eEF1A2 experimental SAS data
CHIMERA model
Sample: Mammalian translation elongation factor eEF1A2 monomer, 50 kDa protein
Buffer: 25 mM Tris HCl, 150 mM NaCl, 6 mM βME, 20% glycerol, 0.01mM GDP,, pH: 7.5
Experiment: SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2023 Mar 21
Dynamics and structural features of the eEF1A1 and eEF1A2 paralogs Nucleic Acids Research 53(21) (2025)
Novosylna O, Shalak V, Dąbrowska K, Patmanidis I, Lozhko D, Bondarchuk T, Schiøtt B, Pedersen J, Knudsen C, Nissen P, Dadlez M, Negrutskii B
RgGuinier 2.6 nm
Dmax 97.1 nm
VolumePorod 60 nm3

SASDXJ2 – Mammalian translation elongation factor eEF1A1

Mammalian translation elongation factor eEF1A1 experimental SAS data
CHIMERA model
Sample: Mammalian translation elongation factor eEF1A1 dimer, 100 kDa protein
Buffer: 25 mM Tris HCl, 150 mM NaCl, 6 mM βME, 20% glycerol, 0.01mM GDP,, pH: 7.5
Experiment: SAXS data collected at Bruker Nanostar w Excillum source, Department of Chemistry, iNANO building, Aarhus Uinversity on 2023 Mar 20
Dynamics and structural features of the eEF1A1 and eEF1A2 paralogs Nucleic Acids Research 53(21) (2025)
Novosylna O, Shalak V, Dąbrowska K, Patmanidis I, Lozhko D, Bondarchuk T, Schiøtt B, Pedersen J, Knudsen C, Nissen P, Dadlez M, Negrutskii B
RgGuinier 4.6 nm
Dmax 143.1 nm
VolumePorod 144 nm3

SASDXB7 – Entamoeba histolytica Anti-Silencing Function 1 (ASF1) with C terminal His6-tag

Anti-Silencing Function 1 experimental SAS data
ALPHAFOLD model
Sample: Anti-Silencing Function 1 monomer, 28 kDa Entamoeba histolytica strain … protein
Buffer: 20 mM Tris, 150 mM NaCl, and 2 mM β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2023 Oct 1
Characterisation of Entamoeba histolytica Anti-Silencing Function 1 as a histone chaperone. Biochimie (2025)
Gandhi S, Vasudevan D
RgGuinier 3.5 nm
Dmax 10.1 nm
VolumePorod 40 nm3

SASDXC7 – Entamoeba histolytica Anti-Silencing Function 1 (ASF1)_Histone H3-H4 dimer complex

Anti-Silencing Function 1Histone H3Histone H4 experimental SAS data
DAMMIF model
Sample: Anti-Silencing Function 1 monomer, 28 kDa Entamoeba histolytica strain … protein
Histone H3 monomer, 15 kDa Entamoeba histolytica strain … protein
Histone H4 monomer, 13 kDa Entamoeba histolytica strain … protein
Buffer: 20 mM Tris, 150 mM NaCl, and 2 mM β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2023 Oct 1
Characterisation of Entamoeba histolytica Anti-Silencing Function 1 as a histone chaperone. Biochimie (2025)
Gandhi S, Vasudevan D
RgGuinier 2.9 nm
Dmax 8.0 nm
VolumePorod 84 nm3

SASDWN5 – N-acetylmuramoyl-L-alanine amidase (without His-Tag)

N-acetylmuramoyl-L-alanine amidase experimental SAS data
COOT model
Sample: N-acetylmuramoyl-L-alanine amidase monomer, 43 kDa Mycobacterium phage DS6A protein
Buffer: 20 mM Tris, 150 mM NaCl and 1 mM DTT, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 Sep 30
Dissecting the molecular basis underlying mycobacterial cell-wall hydrolysis by the catalytic domains of D29LysA and DS6ALysA phage endolysins. Int J Biol Macromol :148896 (2025)
Ceballos-Zúñiga F, Galvez-Larrosa L, Muñoz IG, Infantes L, Fernández-Carrillo J, Pérez-Dorado I
RgGuinier 2.8 nm
Dmax 9.5 nm
VolumePorod 50 nm3

SASDWP5 – N-acetylmuramoyl-L-alanine amidase (with His-Tag)

N-acetylmuramoyl-L-alanine amidase (Mycobacteriophage DS6A) experimental SAS data
COOT model
Sample: N-acetylmuramoyl-L-alanine amidase (Mycobacteriophage DS6A) monomer, 45 kDa protein
Buffer: 20 mM Tris, 150 mM NaCl and 1 mM DTT, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2023 Mar 30
Dissecting the molecular basis underlying mycobacterial cell-wall hydrolysis by the catalytic domains of D29LysA and DS6ALysA phage endolysins. Int J Biol Macromol :148896 (2025)
Ceballos-Zúñiga F, Galvez-Larrosa L, Muñoz IG, Infantes L, Fernández-Carrillo J, Pérez-Dorado I
RgGuinier 2.8 nm
Dmax 10.3 nm
VolumePorod 62 nm3